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Inositol hexakisphosphate kinase-1 interacts with perilipin1 to modulate lipolysis. | LitMetric

Inositol hexakisphosphate kinase-1 interacts with perilipin1 to modulate lipolysis.

Int J Biochem Cell Biol

Department of Metabolism and Aging, The Scripps Research Institute, Jupiter, FL 33458, USA. Electronic address:

Published: September 2016

AI Article Synopsis

Article Abstract

Lipolysis leads to the breakdown of stored triglycerides (TAG) to release free fatty acids (FFA) and glycerol which is utilized by energy expenditure pathways to generate energy. Therefore, a decrease in lipolysis augments fat accumulation in adipocytes which promotes weight gain. Conversely, if lipolysis is not complemented by energy expenditure, it leads to FFA induced insulin resistance and type-2 diabetes. Thus, lipolysis is under stringent physiological regulation, although the precise mechanism of the regulation is not known. Deletion of inositol hexakisphosphate kinase-1 (IP6K1), the major inositol pyrophosphate biosynthetic enzyme, protects mice from high fat diet (HFD) induced obesity and insulin resistance. IP6K1-KO mice are lean due to enhanced energy expenditure. Therefore, IP6K1 is a target in obesity and type-2 diabetes. However, the mechanism/s by which IP6K1 regulates adipose tissue lipid metabolism is yet to be understood. Here, we demonstrate that IP6K1-KO mice display enhanced basal lipolysis. IP6K1 modulates lipolysis via its interaction with the lipolytic regulator protein perilipin1 (PLIN1). Furthermore, phosphorylation of IP6K1 at a PKC/PKA motif modulates its interaction with PLIN1 and lipolysis. Thus, IP6K1 is a novel regulator of PLIN1 mediated lipolysis.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5003629PMC
http://dx.doi.org/10.1016/j.biocel.2016.06.018DOI Listing

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